Descriptor in English: | Myosins |
Descriptor in Spanish: | Miosinas |
Descriptor in Portuguese: | Miosinas |
Descriptor in French: | Myosines |
Entry term(s): |
ATPase, Actin Activated ATPase, Actin-Activated ATPase, Actomyosin ATPase, Myosin Actin Activated ATPase Actin-Activated ATPase Actomyosin ATPase Actomyosin Adenosinetriphosphatase Adenosine Triphosphatase, Myosin Adenosinetriphosphatase, Actomyosin Adenosinetriphosphatase, Myosin Myosin Myosin ATPase Myosin Adenosine Triphosphatase Myosin Adenosinetriphosphatase |
Tree number(s): |
D05.750.078.730.475 D08.811.277.040.025.193.750 D12.776.210.500.600 D12.776.220.525.475 |
Scope note: | A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. |
Annotation: | GEN or unspecified; prefer specifics |
Allowable Qualifiers: |
AD administration & dosage AE adverse effects AI antagonists & inhibitors AN analysis BI biosynthesis BL blood CF cerebrospinal fluid CH chemistry CL classification CS chemical synthesis DE drug effects DF deficiency EC economics GE genetics HI history IM immunology IP isolation & purification ME metabolism PD pharmacology PH physiology PK pharmacokinetics PO poisoning RE radiation effects SD supply & distribution ST standards TO toxicity TU therapeutic use UL ultrastructure UR urine |
History Note: | 2002(1971); use ADENOSINE TRIPHOSPHATASE 1963-1968; for MYOSIN ATPASE use ADENOSINETRIPHOSPHATASE 1984-1988; for ACTOMYOSIN ATPASE use ADENOSINETRIPHOSPHATASE 1985-1988 |
DeCS UI: | 29449 |
Descriptor UI: | D009218 |
Date Established: | 1973/01/01 |
Date of Entry: | 1999/01/01 |
Revision Date: | 2013/07/09 |
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CHEMICALS AND DRUGS
Macromolecular Substances [D05]Macromolecular Substances -
CHEMICALS AND DRUGS
Enzymes and Coenzymes [D08]Enzymes and Coenzymes -
CHEMICALS AND DRUGS
Amino Acids, Peptides, and Proteins [D12]Amino Acids, Peptides, and Proteins -
CHEMICALS AND DRUGS
Amino Acids, Peptides, and Proteins [D12]Amino Acids, Peptides, and Proteins
|
Myosins
- Preferred
Actomyosin Adenosinetriphosphatase
- Related but not broader or narrower
Concept UI |
M0014361 |
Scope note | A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. |
Preferred term | Myosins |
Entry term(s) |
ATPase, Actin Activated ATPase, Actin-Activated ATPase, Myosin Actin Activated ATPase Actin-Activated ATPase Adenosine Triphosphatase, Myosin Adenosinetriphosphatase, Myosin Myosin Myosin ATPase Myosin Adenosine Triphosphatase Myosin Adenosinetriphosphatase |
Concept UI |
M0375356 |
Preferred term | Actomyosin Adenosinetriphosphatase |
Entry term(s) |
ATPase, Actomyosin Actomyosin ATPase Adenosinetriphosphatase, Actomyosin |
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